Regulation of ADAM12 cell-surface expression by protein kinase C epsilon. - Wikidata - wikimedia - TriplyDB

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

http://www.wikidata.org/entity/Q40516107

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Proteomic identification of ADAM12 as a regulator for TGF-β1-induced differentiation of human mesenchymal stem cells to smooth muscle cells Preferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions.Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration.Phospholipid-binding protein EhC2A mediates calcium-dependent translocation of transcription factor URE3-BP to the plasma membrane of Entamoeba histolytica.RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis.Metalloproteinases: key and common mediators of multiple GPCRs and candidate therapeutic targets in models of hypertensive cardiac disease.Functional analysis of a breast cancer-associated mutation in the intracellular domain of the metalloprotease ADAM12 Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).Protein kinase Cepsilon binds peripherin and induces its aggregation, which is accompanied by apoptosis of neuroblastoma cells.Differential surface expression of ADAM10 and ADAM17 on human T lymphocytes and tumor cells.ADAM12 produced by tumor cells rather than stromal cells accelerates breast tumor progression.PKCα mediates acetylcholine-induced activation of TRPV4-dependent calcium influx in endothelial cells.Protein kinase C iota as a therapeutic target in alveolar rhabdomyosarcoma.Identification of ILK as a new partner of the ADAM12 disintegrin and metalloprotease in cell adhesion and survival Molecular and cellular mechanisms of ectodomain shedding Protein kinase Cθ C2 domain is a phosphotyrosine binding module that plays a key role in its activation.Insights into ectodomain shedding and processing of protein-tyrosine pseudokinase 7 (PTK7)Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzyme ADAM12-cleaved ephrin-A1 contributes to lung metastasis.γ-Secretase Dependent Nuclear Targeting of Dystroglycan.Cooperation of the metalloprotease, disintegrin, and cysteine-rich domains of ADAM12 during inhibition of myogenic differentiation.Proteomic screening identifies the zonula occludens protein ZO-1 as a new partner for ADAM12 in invadopodia-like structures.ADAM12 Is a Four-leafed Clover

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Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

http://www.wikidata.org/entity/Q40516107

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

@zh-cn

name

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

@en

type

label

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

@en

prefLabel

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

@en

P1433

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P1433

Journal of Biological Chemistry

P1476

Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.

@en

P2093

Charles Kumar Thodeti

http://www.w3.org/2001/XMLSchema#string

Christer Larsson

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Christina Sundberg

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Marie Kveiborg

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Peter Parker

http://www.w3.org/2001/XMLSchema#string

Reidar Albrechtsen

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Ulla M Wewer

http://www.w3.org/2001/XMLSchema#string

P2860

Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion

TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells

A metalloprotease-disintegrin participating in myoblast fusion

A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo

Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding.

A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.

ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading

ADAM 12 protease induces adipogenesis in transgenic mice

A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

P304

51601-51611

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scholarly article

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10.1074/JBC.M403753200

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49

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279

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P577

2004-09-13T00:00:00Z

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P698

15364951

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